Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Synovial fluid was found to contain an inhibitor of neutrophil chemotaxis. The activity of this inhibitor was masked in native synovial fluid, but could be detected in fluid in which complement had been deactivated by mild heating. The inhibitor was most effective against the chemotactic activity of zymosan-activated serum (C5ades arg). It had little effect when N-formyl-methionyl-leucyl-phenylalanine served as chemoattractant. Inhibition was not the result of a direct effect on the neutrophils, since incubation of cells with synovial fluid did not alter their chemotactic response. The inhibitory activity was destroyed by boiling the synovial fluid or treating it with trypsin, suggesting that it is a protein (or proteins); it was not affected by hyaluronidase treatment. Gel filtration revealed that the inhibitor was present in native as well as decomplemented synovial fluid, and that its molecular weight was in the vicinity of 25,000. It is proposed that this inhibitory activity plays a role in the regulation of the inflammatory response in joints.
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PMID:A chemotactic inhibitor in synovial fluid. 684 Aug 1

Two factors from normal rat liver cytoplasm inhibited the proliferation of cultured L-929 fibroblasts. One was arginase, the other was a small molecular weight inhibitor stable to trypsin and heat treatment. The small molecular weight inhibitor inhibited the protein and DNA synthesis of L-cells. Inhibition of DNA synthesis was thought to be secondary to the inhibition of protein synthesis.
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PMID:Factors inhibiting cell proliferation in rat liver cytoplasm. 706 29

Five protease inhibitors were isolated from peanut seeds and named A-I, A-II, B-I, B-II, and B-III. These inhibitors seemed to be Bowman-Birk type inhibitors judging from their low molecular weights and high cystine contents. All the inhibitors inhibited both bovine trypsin and chymotrypsin at ratios of 1:2 and 1:1, respectively, but not simultaneously. The complexes of the inhibitors and trypsin no longer inhibit chymotrypsin. On the other hand, their complexes with chymotrypsin inhibit trypsin with a slow release of chymotrypsin.
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PMID:Purification and characterization of protease inhibitors from peanuts (Arachis hypogaea). 709 96

Methods were developed for the peptide analysis of individual isoproteins of human apolipoproteins separated on urea-polyacrylamide isoelectric focusing (IEF) gels. After IEF the proteins were fixed in the gel matrix by trichloroacetic acid precipitation. Low molecular weight contaminants, including ampholytes, were removed and the proteins were chemically desialylated. Enzymatic digestions with L-1-tosyl-2-phenylethylchloromethyl ketone - trypsin, chymotrypsin, or with thermolysin were accomplished within the gel matrix. The proteolytically released peptides were analyzed by reverse-phase high performance liquid chromatography. These methods facilitated the comprehensive analysis of protein structural differences between individual isoproteins of apolipoproteins in duplicate with as little as 1-2 nmol of each isoprotein, without the use of radiolabels. Human apolipoproteins A-I, C, and E were analysed by these methods.
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PMID:Analysis of enzymatically released peptides by reverse-phase high performance liquid chromatography from picomole amounts of apolipoproteins separated on polyacrylamide isoelectric focusing gels. 712 86

Controversial results have been published as to the presence of arginase activity in human skin fibroblasts in normal cells and in argininemia. Experiments were undertaken to see if arginase is intrinsic to the fibroblasts or may be there as the result of exogenous contamination inherent to the mode of cell culturing. The mode of harvesting by scraping or trypsin treatment demonstrated similar arginase activity. No significant differences of arginase activity were found between the fibroblasts grown on fetal calf or human serum. In the conditioned serum-free medium arginase separated on DEAE-cellulose into an A1 and A4 form. These fractions are identical with those found in the cells. Arginase activity varies, however, with age of the fibroblasts. These observations are also valid for fibroblasts from a case of argininemia. Arginase activity is therefore intrinsic to diploid human fibroblasts.
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PMID:Arginase activity in human fibroblast cultures. 726 9

The influence of a raw green gram (RGG) diet, an autoclaved green gram (AGG) diet and green gram trypsin inhibitors (GGTI) incorporated in AGG diet on urinary and blood urea and creatinine levels in rats was studied. The activities of certain liver enzymes of pathways associated with protein or amino acid metabolism were also studied. The levels of urea and creatinine in urine and blood were found to be significantly increased in rats fed the RGG and GGTI-incorporated AGG diets when compared to the animals fed with the AGG diet. The levels of enzyme activities of arginase, ornithine transcarbamoylase, aspartate aminotransferase and alanine aminotransferase were also found to be significantly increased along with that of urea and creatinine, The possible role of GGTI on the altered levels of the above-mentioned parameters is discussed.
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PMID:Influence of dietary raw green gram (Phaseolus aureus Roxb) and green gram trypsin inhibitors on the activity of certain protein metabolism enzymes in rats. 733 25

We investigated the effects of the thrombin inhibitor, argatroban ((2R,4R)-4-methyl-1-[N2-(3-methyl-1,2,3,4-tetrahydro-8- quinolinesulfonyl)-L-arginyl]-2-piperidinecarboxylic acid) on the endothelium-derived relaxing factor-nitric oxide (EDRF-NO)-dependent relaxant, and the endothelial cell-independent constrictor actions of thrombin. Experiments were performed in isolated rings of canine coronary arteries. Argatroban inhibited thrombin-induced relaxation (range of thrombin activity 0.003-0.3 U/ml), with an ED50 of 0.3 microM. The ED50 value was not different from inhibition of thrombin amidolytic cleavage of the chromogenic substrate N-p-tosylgly-pro-arg-p-nitroanilide acetate (TOGSPAN 0.28 microM), but inhibition was highly selective. Argatroban did not block EDRF-NO-dependent relaxations to trypsin (0.003-0.3 U/ml; Emax -88.7 + 2.0% without vs. -88.1 +/- 2.7% with argatroban), acetylcholine (ACh 1 nM to 1 microM; Emax -90.5 +/- 4.7% and -88.6 +/- 3.1%, with and without argatroban, respectively), or the calcium ionophore A23187 (1 nM to 1 microM; Emax -98.5 +/- 1.2 vs. -99.4 +/- 0.6%). The inhibitory effects of argatroban on thrombin-induced constriction were then compared with those of the irreversible thrombin inhibitor D-phenylalanyl-L-prolyl L-arginine chloromethyl ketone (PPACK). The highest concentration of argatroban (10 microM) inhibited the vasoconstrictor effects of thrombin but did not completely block the effects (Emax 21.4 +/- 8.1% of KCl constriction without argatroban and Emax 14.0 +/- 5.2% of KCl-induced constriction with argatroban). In contrast, both a 10- and a 100-fold lower concentration of PPACK (0.1-1 microM) prevented the thrombin-induced increase in tension. Thrombin-induced constriction therefore appeared to disclose mechanistic differences between the two thrombin inhibitors. Thrombin vasomotor actions were inhibited by argatroban, however, and this may contribute significantly to the therapeutic effect of argatroban.
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PMID:Argatroban and inhibition of the vasomotor actions of thrombin. 750 29

As determined by atomic absorption, fully activated human liver arginase contained 1.1 +/- 0.1 Mn2+/subunit. Upon dissociation to inactive subunits (< 0.01 Mn2+/subunit), there was decreased intensity and a red shift in the tryptophan fluorescence emission spectra of the enzyme, and the resulting species were markedly sensitive to thermal and proteolytic inactivation by trypsin. Arginine and lysine specifically protected the subunits from heat inactivation. Subunit activation by Mn2+ followed hyperbolic kinetics (Kd = 0.08 +/- 0.01 microM). In addition to Mn2+, Ni2+ and Co2+ converted inactive subunits into active monomers, and favoured their association to the oligomeric state of the enzyme (M(r) = 120,000 +/- 2000). The replacement of Mn2+ by Ni2+ or Co2+ resulted in significant changes in Vmax without any change in the Km values for the substrates (arginine or canavanine) or the Ki value for lysine inhibition. The results support our previous suggestion (Carvajal et al., 1994) that Mn2+ is not essential for substrate binding to arginase, and substantiates the conclusion that species differences may exist in the interaction of arginase with metal ions.
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PMID:Interaction of arginase with metal ions: studies of the enzyme from human liver and comparison with other arginases. 758 44

Treponema denticola (Td) and Porphyromonas gingivalis (Pg) are associated with human moderate and severe adult periodontal diseases. This study quantifies these two anaerobes and their trypsin-like (TL) activities in subgingival plaque collected from both clinically healthy and periodontally diseased sites of human periodontitis patients. Antigen levels of the microorganisms were determined by monoclonal antibodies and TL activities were measured by the fluorescent substrate Z-gly-gly-arg-AFC in a disc format. Significant positive correlations were observed between the antigen levels and the TL activities when the data were subjected to statistical analyses both on a site-specific and on a patient basis. Anaerobe synergism was found between Td and Pg in a continental US population, and positive correlations were found between anaerobe levels (individually and total) and clinical indicators of adult periodontitis.
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PMID:Trypsin-like activity levels of Treponema denticola and Porphyromonas gingivalis in adults with periodontitis. 798 15

A high level of the membrane-bound proteinase (LMP) secretion by human polymorphonuclear leukocytes (up to 680 nmol/min/ml with N-benzoyl-L-arg-EE as a substrate) was shown during the cell adhesion to receptor-dependent (immobilized aggregates of IgG and C3b) and receptor-independent (DEAE-Sephadex and polymethyl methacrylate) absorbents. Incubation medium contained 6.10(6) cells/ml. The rate of secretion reached the maximal level during 15 min although its level was already high to the 5 min of C3b- and hydrophobic surface-induced activation (491 +/- 55 and 382 nmol/min, respectively). The high level of LMP secretion coincided with the peak of luminol-dependent chemoluminescence during the receptor-dependent adhesion, but did not correlate with a low level of luminescence in the receptor-independent adhesion. Localization of LMP in latent form in neutrophil membrane was shown earlier; the enzyme activation may occur due to effect of polycationic molecules of bovine tissue proteinase inhibitor of Kunitz type, protamine sulfate, alkaline fraction of ampholines. The enzyme (with BAEE as a substrate) was identified as serine proteinase of the trypsin-like type which activated Hageman factor (the XII factor of clotting system) and demonstrated the kininogenase activity. Only slight elastase-like activity was detected after incubation of neutrophils with all the adsorbents studied (0-2 nmol/min/ml with MeOSucAlaAlaProValpNA as a substrate). Chymotrypsin-like activity achieved maximum only by 30 min of activation with all the types of adsorbents (up to 270 nmol/min/ml with N-benzoyl-Tyr-EE as a substrate); this suggests impairment of azurophilic granules and appearance of cathepsin G.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Secretion of membrane-bound serine proteinases by polymorphonuclear leukocytes during adhesion to various types of receptor-dependent and receptor-independent sorbents]. 807 31


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